This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The herpes simplex type-1 virus capsid has a diameter of 1250 [unreadable] and is made up of 4 distinct structural proteins (VP5, VP23, Vp19C and VP26) and a portal complex with a total mass of ~192 MDa. We completed its structure at 8.5 [unreadable] resolution. This represents the largest virus particle solved structurally to such a high resolution. Since then, we have developed a comprehensive approach to study this viral capsid in more detail by a combination of structural prediction, crystallography, single particle reconstruction and electron cryo-tomography.